ID   3SIH_DENJJ              Reviewed;          84 AA.
AC   P0DQP2;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   07-APR-2021, sequence version 1.
DT   25-MAY-2022, entry version 4.
DE   RecName: Full=Venom protein SynTx {ECO:0000303|PubMed:33000863};
DE   AltName: Full=Dj_SynTx {ECO:0000303|PubMed:33000863};
DE   AltName: Full=Synergistic-like venom 3FTx protein S2C4 homolog {ECO:0000303|PubMed:28843532};
DE   AltName: Full=T3431 {ECO:0000303|PubMed:28843532};
DE   Flags: Precursor; Fragment;
OS   Dendroaspis jamesoni jamesoni (Jameson's mamba).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Elapinae; Dendroaspis.
OX   NCBI_TaxID=2032609;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Venom gland;
RX   PubMed=28843532; DOI=10.1016/j.jprot.2017.08.016;
RA   Ainsworth S., Petras D., Engmark M., Suessmuth R.D., Whiteley G.,
RA   Albulescu L.O., Kazandjian T.D., Wagstaff S.C., Rowley P., Wuester W.,
RA   Dorrestein P.C., Arias A.S., Gutierrez J.M., Harrison R.A., Casewell N.R.,
RA   Calvete J.J.;
RT   "The medical threat of mamba envenoming in sub-Saharan Africa revealed by
RT   genus-wide analysis of venom composition, toxicity and antivenomics
RT   profiling of available antivenoms.";
RL   J. Proteomics 172:173-189(2018).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-84, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 20-84.
RC   TISSUE=Venom;
RX   PubMed=33000863; DOI=10.1042/bcj20200529;
RA   Aoki-Shioi N., Jobichen C., Sivaraman J., Kini R.M.;
RT   "Unusual quaternary structure of a homodimeric synergistic-type toxin from
RT   mamba snake venom defines its molecular evolution.";
RL   Biochem. J. 477:3951-3962(2020).
CC   -!- FUNCTION: This protein shows a synergetic toxic effect in that it
CC       enhances the toxicity of other toxins. {ECO:0000250|UniProtKB:P01407}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:33000863}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:33000863}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:33000863}.
CC   -!- MASS SPECTROMETRY: Mass=7584.7; Method=Electrospray; Note=Homodimer
CC       mass is 14,122.9.; Evidence={ECO:0000269|PubMed:33000863};
CC   -!- MISCELLANEOUS: Is classified as a P-type cytotoxin, since a proline
CC       residue stands at position 32 (Pro-31 in standard classification).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Short-chain
CC       subfamily. Aminergic toxin sub-subfamily. {ECO:0000305}.
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DR   PDB; 7C28; X-ray; 2.40 A; A/B=20-84.
DR   PDBsum; 7C28; -.
DR   AlphaFoldDB; P0DQP2; -.
DR   SMR; P0DQP2; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   CDD; cd00206; snake_toxin; 1.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR003572; Cytotoxin_Cobra.
DR   InterPro; IPR003571; Snake_3FTx.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR018354; Snake_toxin_con_site.
DR   InterPro; IPR035076; Toxin/TOLIP.
DR   Pfam; PF00087; Toxin_TOLIP; 1.
DR   PRINTS; PR00282; CYTOTOXIN.
DR   SUPFAM; SSF57302; SSF57302; 1.
DR   PROSITE; PS00272; SNAKE_TOXIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Secreted; Signal;
KW   Toxin.
FT   SIGNAL          <1..19
FT                   /evidence="ECO:0000305"
FT   CHAIN           20..84
FT                   /note="Venom protein SynTx"
FT                   /evidence="ECO:0000269|PubMed:33000863"
FT                   /id="PRO_0000452284"
FT   DISULFID        22..43
FT                   /evidence="ECO:0000269|PubMed:33000863,
FT                   ECO:0007744|PDB:7C28"
FT   DISULFID        36..61
FT                   /evidence="ECO:0000269|PubMed:33000863,
FT                   ECO:0007744|PDB:7C28"
FT   DISULFID        65..76
FT                   /evidence="ECO:0000269|PubMed:33000863,
FT                   ECO:0007744|PDB:7C28"
FT   DISULFID        73
FT                   /note="Interchain"
FT                   /evidence="ECO:0000269|PubMed:33000863,
FT                   ECO:0007744|PDB:7C28"
FT   DISULFID        77..82
FT                   /evidence="ECO:0000269|PubMed:33000863,
FT                   ECO:0007744|PDB:7C28"
FT   NON_TER         1
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   84 AA;  9101 MW;  95435518803DAAE3 CRC64;
     TLLLTLVVVT IVCLDLGYTL TCVTDKSFGG VITEECAAGQ KICFKNWKKM GPKLYDVKRG
     CTATCPKADD NGCVKCCNTD KCNK